ID DHSA_SCHPO Reviewed; 641 AA. AC Q9UTJ7; P78912; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 08-MAR-2011, entry version 79. DE RecName: Full=Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial; DE EC=1.3.5.1; DE AltName: Full=Flavoprotein subunit of complex II; DE Short=FP; DE Flags: Precursor; GN Name=sdh1; ORFNames=SPAC1556.02c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 38366 / 972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-641. RC STRAIN=PR745; RX MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363; RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.; RT "Identification of open reading frames in Schizosaccharomyces pombe RT cDNAs."; RL DNA Res. 4:363-369(1997). CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase CC (SDH) that is involved in complex II of the mitochondrial electron CC transport chain and is responsible for transferring electrons from CC succinate to ubiquinone (coenzyme Q) (By similarity). CC -!- CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol. CC -!- COFACTOR: FAD (By similarity). CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC fumarate from succinate (eukaryal route): step 1/1. CC -!- SUBUNIT: Component of complex II composed of four subunits: a CC flavoprotein (FP), an iron-sulfur protein (IP), and a cytochrome b CC composed of a large and a small subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral CC membrane protein; Matrix side (By similarity). CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU329670; CAB61213.1; -; Genomic_DNA. DR EMBL; D89263; BAA13924.1; -; mRNA. DR PIR; T50081; T50081. DR ProteinModelPortal; Q9UTJ7; -. DR SMR; Q9UTJ7; 47-641. DR STRING; Q9UTJ7; -. DR EnsemblFungi; SPAC1556.02c-1; SPAC1556.02c-1; SPAC1556.02c. DR GenomeReviews; CU329670_GR; sdh1. DR KEGG; spo:SPAC1556.02c; -. DR NMPDR; fig|4896.1.peg.4289; -. DR GeneDB_Spombe; SPAC1556.02c; -. DR eggNOG; fuNOG04691; -. DR GeneTree; EFGT00050000001028; -. DR HOGENOM; HBG293998; -. DR OMA; ALGNSHE; -. DR OrthoDB; EOG41G6C9; -. DR PhylomeDB; Q9UTJ7; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-002428-MONOMER; -. DR BRENDA; 1.3.5.1; 653. DR ArrayExpress; Q9UTJ7; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:EC. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006105; P:succinate metabolic process; IC:GeneDB_Spombe. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR003953; FAD_bind2_N. DR InterPro; IPR003952; FRD_SDH_FAD_BS. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR004112; Fum_Rdtase/Succ_DH_flav_C. DR InterPro; IPR011281; Succ_DH_flav_su_fwd. DR InterPro; IPR014006; Succ_Dhase_frdA_Gneg. DR Gene3D; G3DSA:1.20.58.100; Fum_Rdtase/Succ_DH_flav-like_C; 1. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR SUPFAM; SSF46977; Succ_DH_flav_C; 1. DR TIGRFAMs; TIGR01816; sdhA_forward; 1. DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1. DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1. PE 2: Evidence at transcript level; KW Complete proteome; Electron transport; FAD; Flavoprotein; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Transit peptide; Transport; Tricarboxylic acid cycle. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 641 Probable succinate dehydrogenase FT [ubiquinone] flavoprotein subunit, FT mitochondrial. FT /FTId=PRO_0000010341. FT NP_BIND 61 66 FAD (By similarity). FT NP_BIND 84 99 FAD (By similarity). FT NP_BIND 450 451 FAD (By similarity). FT ACT_SITE 333 333 Proton acceptor (By similarity). FT BINDING 268 268 FAD (By similarity). FT BINDING 289 289 Substrate (By similarity). FT BINDING 301 301 Substrate (By similarity). FT BINDING 400 400 Substrate (By similarity). FT BINDING 434 434 FAD (By similarity). FT BINDING 445 445 Substrate (By similarity). FT MOD_RES 92 92 Tele-8alpha-FAD histidine (By FT similarity). FT CONFLICT 214 214 A -> G (in Ref. 2; BAA13924). FT CONFLICT 218 218 I -> L (in Ref. 2; BAA13924). SQ SEQUENCE 641 AA; 70466 MW; 5E5FCD857C372199 CRC64; MLRFRKVAPS LKNGGNLKLF STSSTLKKIA SSQPLRAKQV STSESVKYPV IDHTYDAIVV GAGGAGLRAT FGLAEAGFNT ACITKLFPTR SHTVAAQGGI NAALGNMTKD DWRWHFYDTV KGSDWLGDQD AIHYMTKEAP KAVLELEHFG VPFSRTKEGK IYQRAFGGQS LEYGKGGQAY RCAAVADRTG HSILHTLYGQ SLKHNTNFFI EYFAMDLIME GGECRGVIAM NLEDGSIHRF RAHKTILATG GYGRAYFSCT SAHTCTGDGN AMVSRAGLPL QDLEFVQFHP TGIYGAGCLI TEGCRGEGGY LLNSKGERFM ERYAPTAKDL ASRDVVSRAM TVEIREGRGV GPEKDHCYLQ LSHLPAEILK ERLPGISETA AIFAGVDVTK EPIPVLPTVH YNMGGIPTRF TGEVLTIDEN GKDKIVPGLY AAGEAACVSV HGGNRLGANS LLDIVVFGRA CALHIKDTLE PNTPHKPLAA DAGLDSLKFL DQIRTSQGPK HTSEIRLDMQ KTMQRDVSVF RMEETLQEGV KNIARVDGTY KDIGIRDRGL IWNTDLVEAL ELRNLLTCAV QTANAALNRK ESRGAHARED YPERDDKNWI KHTLTWQHKT GDPVTLKYRA VTRTTMDENE VKPVPPFKRV Y //